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Protein

Microtubule-associated protein 1B

Gene

MAP1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing.By similarity1 Publication

GO - Molecular functioni

  • structural molecule activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131711-MONOMER.
SIGNORiP46821.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Cleaved into the following 2 chains:
Gene namesi
Name:MAP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6836. MAP1B.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: HPA
  • cytosol Source: Ensembl
  • dendritic spine Source: UniProtKB-SubCell
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: ProtInc
  • photoreceptor outer segment Source: Ensembl
  • plasma membrane Source: DFLAT
  • postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Microtubule, Synapse

Pathology & Biotechi

Organism-specific databases

DisGeNETi4131.
OpenTargetsiENSG00000131711.
PharmGKBiPA30581.

Chemistry databases

ChEMBLiCHEMBL3217382.

Polymorphism and mutation databases

BioMutaiMAP1B.
DMDMi317373388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000186042 – 2468Microtubule-associated protein 1BAdd BLAST2467
ChainiPRO_00004183792 – 2206MAP1B heavy chainAdd BLAST2205
ChainiPRO_00000186052207 – 2468MAP1 light chain LC1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei336PhosphoserineCombined sources1
Modified residuei339PhosphoserineBy similarity1
Modified residuei343PhosphoserineCombined sources1
Modified residuei527PhosphothreonineBy similarity1
Modified residuei541PhosphoserineCombined sources1
Modified residuei544PhosphoserineBy similarity1
Modified residuei561PhosphoserineBy similarity1
Modified residuei614PhosphoserineCombined sources1
Modified residuei828PhosphoserineCombined sources1
Modified residuei831PhosphoserineCombined sources1
Modified residuei832PhosphoserineCombined sources1
Modified residuei891PhosphoserineBy similarity1
Modified residuei899PhosphothreonineBy similarity1
Modified residuei908PhosphothreonineBy similarity1
Modified residuei936PhosphoserineBy similarity1
Modified residuei937PhosphoserineCombined sources1
Modified residuei948PhosphothreonineCombined sources1
Modified residuei970PhosphoserineBy similarity1
Modified residuei977PhosphoserineBy similarity1
Modified residuei992PhosphoserineCombined sources1
Modified residuei995PhosphoserineCombined sources1
Modified residuei1016PhosphoserineCombined sources1
Modified residuei1144PhosphoserineCombined sources1
Modified residuei1154PhosphoserineCombined sources1
Modified residuei1156PhosphoserineCombined sources1
Modified residuei1187PhosphoserineBy similarity1
Modified residuei1190PhosphoserineBy similarity1
Modified residuei1208PhosphoserineCombined sources1
Modified residuei1211PhosphoserineBy similarity1
Modified residuei1212PhosphoserineBy similarity1
Modified residuei1229PhosphoserineBy similarity1
Modified residuei1247PhosphoserineBy similarity1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1256PhosphoserineCombined sources1
Modified residuei1258PhosphoserineBy similarity1
Modified residuei1260PhosphoserineCombined sources1
Modified residuei1262PhosphoserineCombined sources1
Modified residuei1265PhosphoserineCombined sources1
Modified residuei1276PhosphoserineCombined sources1
Modified residuei1280PhosphoserineCombined sources1
Modified residuei1282PhosphothreonineCombined sources1
Modified residuei1298PhosphoserineCombined sources1
Modified residuei1312PhosphoserineBy similarity1
Modified residuei1322PhosphoserineCombined sources1
Modified residuei1324PhosphoserineBy similarity1
Modified residuei1326PhosphoserineBy similarity1
Modified residuei1328PhosphothreonineBy similarity1
Modified residuei1330PhosphoserineBy similarity1
Modified residuei1339PhosphoserineBy similarity1
Modified residuei1376PhosphoserineBy similarity1
Modified residuei1378PhosphoserineCombined sources1
Modified residuei1387PhosphoserineCombined sources1
Modified residuei1389PhosphoserineCombined sources1
Modified residuei1396PhosphoserineCombined sources1
Modified residuei1400PhosphoserineCombined sources1
Modified residuei1408PhosphoserineBy similarity1
Modified residuei1410PhosphotyrosineBy similarity1
Modified residuei1427PhosphoserineCombined sources1
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1443PhosphoserineCombined sources1
Modified residuei1501PhosphoserineCombined sources1
Modified residuei1512PhosphoserineBy similarity1
Modified residuei1520PhosphoserineBy similarity1
Modified residuei1522PhosphoserineBy similarity1
Modified residuei1525PhosphothreonineBy similarity1
Modified residuei1527PhosphoserineBy similarity1
Modified residuei1618PhosphoserineCombined sources1
Modified residuei1620PhosphoserineCombined sources1
Modified residuei1625PhosphoserineCombined sources1
Modified residuei1653PhosphoserineCombined sources1
Modified residuei1663PhosphoserineBy similarity1
Modified residuei1666PhosphoserineCombined sources1
Modified residuei1690PhosphoserineBy similarity1
Modified residuei1772PhosphoserineBy similarity1
Modified residuei1779PhosphoserineCombined sources1
Modified residuei1782PhosphoserineCombined sources1
Modified residuei1785PhosphoserineCombined sources1
Modified residuei1788PhosphothreonineCombined sources1
Modified residuei1792PhosphoserineBy similarity1
Modified residuei1793PhosphoserineCombined sources1
Modified residuei1796PhosphotyrosineBy similarity1
Modified residuei1797PhosphoserineCombined sources1
Modified residuei1801PhosphoserineBy similarity1
Modified residuei1819PhosphoserineBy similarity1
Modified residuei1881PhosphoserineBy similarity1
Modified residuei1899PhosphoserineCombined sources1
Modified residuei1915PhosphoserineCombined sources1
Modified residuei1917PhosphoserineCombined sources1
Modified residuei1919PhosphoserineCombined sources1
Modified residuei1932PhosphothreonineCombined sources1
Modified residuei1939PhosphoserineCombined sources1
Modified residuei1949PhosphothreonineCombined sources1
Modified residuei1965PhosphoserineCombined sources1
Modified residuei2034PhosphothreonineCombined sources1
Modified residuei2209PhosphoserineCombined sources1
Modified residuei2271PhosphoserineCombined sources1
Modified residuei2289PhosphoserineCombined sources1
Modified residuei2305PhosphothreonineCombined sources1
Modified residuei2414PhosphoserineBy similarity1
Modified residuei2464S-nitrosocysteineBy similarity1

Post-translational modificationi

LC1 is generated from MAP1B by proteolytic processing.1 Publication
S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP46821.
MaxQBiP46821.
PaxDbiP46821.
PeptideAtlasiP46821.
PRIDEiP46821.

PTM databases

iPTMnetiP46821.
PhosphoSitePlusiP46821.

Expressioni

Gene expression databases

BgeeiENSG00000131711.
CleanExiHS_MAP1B.
ExpressionAtlasiP46821. baseline and differential.
GenevisibleiP46821. HS.

Organism-specific databases

HPAiCAB009792.
HPA022275.

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL (By similarity). Interacts (via C-terminus) with GAN (via Kelch domains) (PubMed:12147674, PubMed:16227972). Interacts (via N-terminus) with DAPK1 (PubMed:18195017). Interacts with TMEM185A (PubMed:15525354). Interacts with MAP1LC3B (PubMed:24089205). Interacts with KIRREL3 (PubMed:25902260).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GANQ9H2C03EBI-764611,EBI-764342
LRRK2Q5S0075EBI-9517186,EBI-5323863
TP53P046376EBI-764611,EBI-366083

Protein-protein interaction databases

BioGridi110304. 58 interactors.
DIPiDIP-33474N.
IntActiP46821. 32 interactors.
MINTiMINT-243072.
STRINGi9606.ENSP00000296755.

Structurei

3D structure databases

ProteinModelPortaliP46821.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1878 – 1894MAP1B 1Add BLAST17
Repeati1895 – 1911MAP1B 2Add BLAST17
Repeati1912 – 1928MAP1B 3Add BLAST17
Repeati1929 – 1945MAP1B 4Add BLAST17
Repeati1946 – 1962MAP1B 5Add BLAST17
Repeati1963 – 1979MAP1B 6Add BLAST17
Repeati1997 – 2013MAP1B 7Add BLAST17
Repeati2014 – 2030MAP1B 8Add BLAST17
Repeati2031 – 2047MAP1B 9Add BLAST17
Repeati2048 – 2064MAP1B 10Add BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2294 – 2468Mediates interaction with TMEM185A1 PublicationAdd BLAST175

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi589 – 790Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add BLAST202

Domaini

Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP46821.
KOiK10429.
OMAiGYSYETI.
OrthoDBiEOG091G12OH.
PhylomeDBiP46821.
TreeFamiTF350229.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamiPF00414. MAP1B_neuraxin. 5 hits.
[Graphical view]
PROSITEiPS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE
60 70 80 90 100
HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL
110 120 130 140 150
HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL
160 170 180 190 200
ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN
210 220 230 240 250
LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT
260 270 280 290 300
SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH
310 320 330 340 350
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI
360 370 380 390 400
SPDLGVVFLN VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR
410 420 430 440 450
SVGNTIDPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE
460 470 480 490 500
FILPNGQEVD LPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE
510 520 530 540 550
GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD SRESLKPAAK
560 570 580 590 600
PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP
610 620 630 640 650
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK
660 670 680 690 700
EEKEKPKKEV AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV
710 720 730 740 750
KKETPPKEVK KEVKKEEKKE VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK
760 770 780 790 800
KPAALKPKVP KKEESVKKDS VAAGKPKEKG KIKVIKKEGK AAEAVAAAVG
810 820 830 840 850
TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF EELKAEEVDV
860 870 880 890 900
TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE
910 920 930 940 950
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE
960 970 980 990 1000
AEEPEEDGEE HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA
1010 1020 1030 1040 1050
EEDMDEAIEK GEAEQSEEEA DEEDKAEDAR EEEYEPEKME AEDYVMAVVD
1060 1070 1080 1090 1100
KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE PASSIHDETL PGGSESEATA
1110 1120 1130 1140 1150
SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR DVMSDETNNE
1160 1170 1180 1190 1200
ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY
1210 1220 1230 1240 1250
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK
1260 1270 1280 1290 1300
VSPSKSPSLS PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE
1310 1320 1330 1340 1350
VTQEVVEEHC ASPEDKTLEV VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT
1360 1370 1380 1390 1400
EVIEKPPAVP VSFEFSDAKD ENERASVSPM DEPVPDSESP IEKVLSPLRS
1410 1420 1430 1440 1450
PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD QVSPVSEMTS
1460 1470 1480 1490 1500
TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV
1510 1520 1530 1540 1550
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA
1560 1570 1580 1590 1600
SVSTASVATS SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT
1610 1620 1630 1640 1650
FQETEMSPSK EECPRPMSIS PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG
1660 1670 1680 1690 1700
QESPEQSLAM DFSRQSPDHP TVGAGVLHIT ENGPTEVDYS PSDMQDSSLS
1710 1720 1730 1740 1750
HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ IASPLQEDTL
1760 1770 1780 1790 1800
SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF
1810 1820 1830 1840 1850
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD
1860 1870 1880 1890 1900
LSTPGLEKDS GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD
1910 1920 1930 1940 1950
VGGYYYEKIE RTTKSPSDSG YSYETIGKTT KTPEDGDYSY EIIEKTTRTP
1960 1970 1980 1990 2000
EEGGYSYDIS EKTTSPPEVS GYSYEKTERS RRLLDDISNG YDDSEDGGHT
2010 2020 2030 2040 2050
LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY CYETAEKITR
2060 2070 2080 2090 2100
TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS
2110 2120 2130 2140 2150
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV
2160 2170 2180 2190 2200
SESAPSQTDS DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP
2210 2220 2230 2240 2250
PPAPVQDRSP SPRHPDVSMV DPEALAIEQN LGKALKKDLK EKTKTKKPGT
2260 2270 2280 2290 2300
KTKSSSPVKK SDGKSKPLAA SPKPAGLKES SDKVSRVASP KKKESVEKAA
2310 2320 2330 2340 2350
KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG TTKTTKSSAV
2360 2370 2380 2390 2400
PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA
2410 2420 2430 2440 2450
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS
2460
SSTVVMQDES FPACKIEL
Length:2,468
Mass (Da):270,634
Last modified:January 11, 2011 - v2
Checksum:i3FFDCB2E20049A8A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036016326R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs766004582dbSNPEnsembl.1
Natural variantiVAR_036017574V → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs369022142dbSNPEnsembl.1
Natural variantiVAR_024530594I → V.3 PublicationsCorresponds to variant rs1866374dbSNPEnsembl.1
Natural variantiVAR_030347869E → G.Corresponds to variant rs16876070dbSNPEnsembl.1
Natural variantiVAR_0341051296P → L.Corresponds to variant rs34093016dbSNPEnsembl.1
Natural variantiVAR_0561231917S → R.Corresponds to variant rs13153166dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06237 mRNA. Translation: AAA18904.1.
BN001084 mRNA. Translation: CAM06633.1.
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1.
CCDSiCCDS4012.1.
RefSeqiNP_005900.2. NM_005909.4.
UniGeneiHs.335079.

Genome annotation databases

EnsembliENST00000296755; ENSP00000296755; ENSG00000131711.
GeneIDi4131.
KEGGihsa:4131.
UCSCiuc003kbw.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06237 mRNA. Translation: AAA18904.1.
BN001084 mRNA. Translation: CAM06633.1.
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1.
CCDSiCCDS4012.1.
RefSeqiNP_005900.2. NM_005909.4.
UniGeneiHs.335079.

3D structure databases

ProteinModelPortaliP46821.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110304. 58 interactors.
DIPiDIP-33474N.
IntActiP46821. 32 interactors.
MINTiMINT-243072.
STRINGi9606.ENSP00000296755.

Chemistry databases

ChEMBLiCHEMBL3217382.

PTM databases

iPTMnetiP46821.
PhosphoSitePlusiP46821.

Polymorphism and mutation databases

BioMutaiMAP1B.
DMDMi317373388.

Proteomic databases

EPDiP46821.
MaxQBiP46821.
PaxDbiP46821.
PeptideAtlasiP46821.
PRIDEiP46821.

Protocols and materials databases

DNASUi4131.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296755; ENSP00000296755; ENSG00000131711.
GeneIDi4131.
KEGGihsa:4131.
UCSCiuc003kbw.5. human.

Organism-specific databases

CTDi4131.
DisGeNETi4131.
GeneCardsiMAP1B.
HGNCiHGNC:6836. MAP1B.
HPAiCAB009792.
HPA022275.
MIMi157129. gene.
neXtProtiNX_P46821.
OpenTargetsiENSG00000131711.
PharmGKBiPA30581.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP46821.
KOiK10429.
OMAiGYSYETI.
OrthoDBiEOG091G12OH.
PhylomeDBiP46821.
TreeFamiTF350229.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000131711-MONOMER.
SIGNORiP46821.

Miscellaneous databases

ChiTaRSiMAP1B. human.
GeneWikiiMAP1B.
GenomeRNAii4131.
PROiP46821.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131711.
CleanExiHS_MAP1B.
ExpressionAtlasiP46821. baseline and differential.
GenevisibleiP46821. HS.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamiPF00414. MAP1B_neuraxin. 5 hits.
[Graphical view]
PROSITEiPS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP1B_HUMAN
AccessioniPrimary (citable) accession number: P46821
Secondary accession number(s): A2BDK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 11, 2011
Last modified: November 2, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.